Controlling protein action Flashcards

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1
Q

What kind of consequences (diseases) can arise as a result of loss of protein control?

A
  • cancer
  • haemophilia
  • polycytic kidney disease
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2
Q

What is haemophilia?

A

a genetic deficiency in clotting factor VIII which causes increased bleeding and usually affects males

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3
Q

In what ways can protein interactions be controlled?

A
  • expression and degradation
  • interaction domains
  • localisation
  • ligand binding
  • protein switches
  • protein modifications
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4
Q

How can protein activity be controlled by expression and degradation?

A
  • control level of lifetime of protein
  • can be controlled by level transcription
  • level of mRNA and protein can be controlled by regulating degradation
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5
Q

What effect can increasing protein expression have?

A

Increase rates of reaction

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6
Q

What effect can degrading certain amounts of protein expression have?

A

Degrading certain proteins can limit rates of reaction

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7
Q

How can effector ligand binding affect protein action?

A

binding of the ligand molecule induces a conformational change to the protein to either inhibit or activate it.

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8
Q

What kind of ligands control protein action?

A

Competetive inhibitors - Bind to AS in place of activator molecule

Allosteric regulation- Bind to the allosteric site and induce a conformational change of the AS

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9
Q

How does product feedback inhibition control protein action?

A

Product inhibition ensures that the activity of an enzyme is reduced when there is sufficient product for the pathway.

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10
Q

How can allosteric regulation lead to activation of proteins?

A

Ligands binding to a regulatory subunit (allosteric regulation) may lead to them dissociating away from the protein and leave the activated catalytic subunits ready for action.

Eg. Protein kinase A by cAMP

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11
Q

What types of allosteric regulation can control protein action?

A

Feedback inhibition
Activation
Cooperative binding

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12
Q

How does allosteric regulation aid cooperative binding?

A

eg. O2 and Hb
As the ligand binds to the allosteric site, It induces a conformational change in the protein so that its AS has a higher affinity for its other ligands and therefore increases the chances of these sites become activated.

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13
Q

How can interaction domains control protein action?

A

Proteins are often made up of multiple domains ands subunits which interact with a range of mlecules leading to varying actions within a cell.

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14
Q

What examples show interaction domains controlling protein action?

A

Localisation - DNA recruits other proteins
Scaffold proteins - creat signal hubs
Intramolecular binding - Binding of 2 domains in the same molecule can inhibit enzymatic activity

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15
Q

How can localisation of a protein control its action?

A

Proteins controlling specific actions will be found in particular locations where they can work most effectively.

Multiple proteins may be colocated if they share a common pathway.

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16
Q

Give examples of localisation controlling protein aciton

A

Transcription factors will not work in the cytoplasm since DNA is in the nucleus

17
Q

How can protein switches control protein action?

A

Some proteins can be switched on or off depending if they are required or not.

18
Q

What are most protein switches?

A

Hydrolytic enzymes that hydrolyse nucleotide triphosphates such as GTPases or ATPases.

19
Q

How do GTPases act as switches?

A

When carrying out hydrolytic activity they can control intracellular transport, protein synthesis, cell growth.

20
Q

How do ATPases act as switches?

A

Act as transporters moving material or motor protein complexes.

21
Q

How can post translational modifications affect protein action?

A

Covalent modifications increasing protein/proteome complexity which can be reversible or irreversible

22
Q

What effects can PMTs have on proteins?

A

Increase/decrease activity
Localisation
Interaction with other proteins/ligands
Degradation

23
Q

How does phosphorylation control protein action?

A

Covalent addition of a phosphate group to serine, threonine or tyrosine residues..

Adds a double negative charge affecting the protein conformations and their interaction activities.

Often used to activate or deactivate protein signalling pathways

24
Q

What maintains a tight regulation of complex pathways?

A

feedback control